MAN2_DROME
ID MAN2_DROME Reviewed; 1108 AA.
AC Q24451; Q9TYG5; Q9VHD8; Q9VHD9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Alpha-mannosidase 2;
DE EC=3.2.1.114 {ECO:0000269|PubMed:10504337};
DE AltName: Full=Golgi alpha-mannosidase II {ECO:0000303|PubMed:7890162};
DE Short=AMan II;
DE Short=Man II;
DE AltName: Full=Golgi alpha-mannosidase IIa {ECO:0000312|FlyBase:FBgn0011740};
DE AltName: Full=Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase;
GN Name=alpha-Man-IIa {ECO:0000312|FlyBase:FBgn0011740};
GN Synonyms=GmII {ECO:0000303|PubMed:7890162};
GN ORFNames=CG18802 {ECO:0000312|FlyBase:FBgn0011740};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7890162; DOI=10.1016/0378-1119(94)00867-r;
RA Foster J.M., Yudkin B., Lockyer A.E., Roberts D.B.;
RT "Cloning and sequence analysis of GmII, a Drosophila melanogaster homologue
RT of the cDNA encoding murine Golgi alpha-mannosidase II.";
RL Gene 154:183-186(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=10504337; DOI=10.1242/jcs.112.19.3319;
RA Rabouille C., Kuntz D.A., Lockyer A.E., Watson R., Signorelli T.,
RA Rose D.R., van den Heuvel M., Roberts D.B.;
RT "The Drosophila GMII gene encodes a Golgi alpha-mannosidase II.";
RL J. Cell Sci. 112:3319-3330(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the first committed step in the biosynthesis of
CC complex N-glycans. It controls conversion of high mannose to complex N-
CC glycans; the final hydrolytic step in the N-glycan maturation pathway
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-
CC D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] =
CC 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:56052,
CC Rhea:RHEA-COMP:14368, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28729, ChEBI:CHEBI:60615, ChEBI:CHEBI:60625;
CC EC=3.2.1.114; Evidence={ECO:0000269|PubMed:10504337};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10504337}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10504337}.
CC -!- INDUCTION: Inhibited by swainsonine and by copper sulfate.
CC {ECO:0000269|PubMed:10504337}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77652; CAA54732.1; -; mRNA.
DR EMBL; AJ132715; CAA10755.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54375.1; -; Genomic_DNA.
DR EMBL; AY119464; AAM50118.1; -; mRNA.
DR PIR; JC4037; JC4037.
DR RefSeq; NP_524291.2; NM_079567.3.
DR PDB; 1HTY; X-ray; 1.40 A; A=94-1108.
DR PDB; 1HWW; X-ray; 1.87 A; A=94-1108.
DR PDB; 1HXK; X-ray; 1.50 A; A=94-1108.
DR PDB; 1PS3; X-ray; 1.80 A; A=64-1108.
DR PDB; 1QWN; X-ray; 1.20 A; A=76-1108.
DR PDB; 1QWU; X-ray; 2.03 A; A=76-1108.
DR PDB; 1QX1; X-ray; 1.30 A; A=76-1108.
DR PDB; 1R33; X-ray; 1.80 A; A=76-1108.
DR PDB; 1R34; X-ray; 1.95 A; A=76-1108.
DR PDB; 1TQS; X-ray; 1.30 A; A=76-1108.
DR PDB; 1TQT; X-ray; 1.90 A; A=76-1108.
DR PDB; 1TQU; X-ray; 2.03 A; A=76-1108.
DR PDB; 1TQV; X-ray; 2.03 A; A=76-1108.
DR PDB; 1TQW; X-ray; 1.20 A; A=76-1108.
DR PDB; 2ALW; X-ray; 1.86 A; A=76-1108.
DR PDB; 2F18; X-ray; 1.30 A; A=76-1108.
DR PDB; 2F1A; X-ray; 1.45 A; A=76-1108.
DR PDB; 2F1B; X-ray; 1.45 A; A=76-1108.
DR PDB; 2F7O; X-ray; 1.43 A; A=76-1108.
DR PDB; 2F7P; X-ray; 1.28 A; A=76-1108.
DR PDB; 2F7Q; X-ray; 1.85 A; A=76-1108.
DR PDB; 2F7R; X-ray; 1.35 A; A=76-1108.
DR PDB; 2FYV; X-ray; 1.90 A; A=76-1108.
DR PDB; 2OW6; X-ray; 1.19 A; A=76-1108.
DR PDB; 2OW7; X-ray; 1.77 A; A=76-1108.
DR PDB; 3BLB; X-ray; 1.30 A; A=76-1108.
DR PDB; 3BUB; X-ray; 1.38 A; A=76-1108.
DR PDB; 3BUD; X-ray; 1.85 A; A=76-1108.
DR PDB; 3BUI; X-ray; 1.25 A; A=76-1108.
DR PDB; 3BUP; X-ray; 2.03 A; A=76-1108.
DR PDB; 3BUQ; X-ray; 2.01 A; A=76-1108.
DR PDB; 3BVT; X-ray; 1.30 A; A=76-1108.
DR PDB; 3BVU; X-ray; 1.12 A; A=76-1108.
DR PDB; 3BVV; X-ray; 1.30 A; A=76-1108.
DR PDB; 3BVW; X-ray; 1.20 A; A=76-1108.
DR PDB; 3BVX; X-ray; 1.10 A; A=76-1108.
DR PDB; 3CV5; X-ray; 1.60 A; A=76-1108.
DR PDB; 3CZN; X-ray; 1.40 A; A=76-1108.
DR PDB; 3CZS; X-ray; 1.30 A; A=76-1108.
DR PDB; 3D4Y; X-ray; 1.52 A; A=76-1108.
DR PDB; 3D4Z; X-ray; 1.39 A; A=76-1108.
DR PDB; 3D50; X-ray; 1.79 A; A=76-1108.
DR PDB; 3D51; X-ray; 1.43 A; A=76-1108.
DR PDB; 3D52; X-ray; 1.60 A; A=76-1108.
DR PDB; 3DDF; X-ray; 1.20 A; A=76-1108.
DR PDB; 3DDG; X-ray; 1.74 A; A=76-1108.
DR PDB; 3DX0; X-ray; 1.70 A; A=76-1108.
DR PDB; 3DX1; X-ray; 1.21 A; A=76-1108.
DR PDB; 3DX2; X-ray; 1.40 A; A=76-1108.
DR PDB; 3DX3; X-ray; 1.42 A; A=76-1108.
DR PDB; 3DX4; X-ray; 1.38 A; A=76-1108.
DR PDB; 3EJP; X-ray; 1.32 A; A=76-1108.
DR PDB; 3EJQ; X-ray; 1.45 A; A=76-1108.
DR PDB; 3EJR; X-ray; 1.27 A; A=76-1108.
DR PDB; 3EJS; X-ray; 1.35 A; A=76-1108.
DR PDB; 3EJT; X-ray; 1.35 A; A=76-1108.
DR PDB; 3EJU; X-ray; 1.32 A; A=76-1108.
DR PDB; 6RPC; X-ray; 1.69 A; A=76-1108.
DR PDB; 6RQZ; X-ray; 1.53 A; A=76-1108.
DR PDB; 6RRH; X-ray; 2.07 A; A=76-1108.
DR PDB; 6RRJ; X-ray; 1.95 A; A=76-1108.
DR PDB; 6RRN; X-ray; 1.59 A; A=76-1108.
DR PDB; 6RRU; X-ray; 1.90 A; A=76-1108.
DR PDB; 6RRW; X-ray; 2.15 A; A=76-1108.
DR PDB; 6RRX; X-ray; 1.84 A; A=76-1108.
DR PDB; 6RRY; X-ray; 1.86 A; A=76-1108.
DR PDB; 6RS0; X-ray; 1.80 A; A=76-1108.
DR PDBsum; 1HTY; -.
DR PDBsum; 1HWW; -.
DR PDBsum; 1HXK; -.
DR PDBsum; 1PS3; -.
DR PDBsum; 1QWN; -.
DR PDBsum; 1QWU; -.
DR PDBsum; 1QX1; -.
DR PDBsum; 1R33; -.
DR PDBsum; 1R34; -.
DR PDBsum; 1TQS; -.
DR PDBsum; 1TQT; -.
DR PDBsum; 1TQU; -.
DR PDBsum; 1TQV; -.
DR PDBsum; 1TQW; -.
DR PDBsum; 2ALW; -.
DR PDBsum; 2F18; -.
DR PDBsum; 2F1A; -.
DR PDBsum; 2F1B; -.
DR PDBsum; 2F7O; -.
DR PDBsum; 2F7P; -.
DR PDBsum; 2F7Q; -.
DR PDBsum; 2F7R; -.
DR PDBsum; 2FYV; -.
DR PDBsum; 2OW6; -.
DR PDBsum; 2OW7; -.
DR PDBsum; 3BLB; -.
DR PDBsum; 3BUB; -.
DR PDBsum; 3BUD; -.
DR PDBsum; 3BUI; -.
DR PDBsum; 3BUP; -.
DR PDBsum; 3BUQ; -.
DR PDBsum; 3BVT; -.
DR PDBsum; 3BVU; -.
DR PDBsum; 3BVV; -.
DR PDBsum; 3BVW; -.
DR PDBsum; 3BVX; -.
DR PDBsum; 3CV5; -.
DR PDBsum; 3CZN; -.
DR PDBsum; 3CZS; -.
DR PDBsum; 3D4Y; -.
DR PDBsum; 3D4Z; -.
DR PDBsum; 3D50; -.
DR PDBsum; 3D51; -.
DR PDBsum; 3D52; -.
DR PDBsum; 3DDF; -.
DR PDBsum; 3DDG; -.
DR PDBsum; 3DX0; -.
DR PDBsum; 3DX1; -.
DR PDBsum; 3DX2; -.
DR PDBsum; 3DX3; -.
DR PDBsum; 3DX4; -.
DR PDBsum; 3EJP; -.
DR PDBsum; 3EJQ; -.
DR PDBsum; 3EJR; -.
DR PDBsum; 3EJS; -.
DR PDBsum; 3EJT; -.
DR PDBsum; 3EJU; -.
DR PDBsum; 6RPC; -.
DR PDBsum; 6RQZ; -.
DR PDBsum; 6RRH; -.
DR PDBsum; 6RRJ; -.
DR PDBsum; 6RRN; -.
DR PDBsum; 6RRU; -.
DR PDBsum; 6RRW; -.
DR PDBsum; 6RRX; -.
DR PDBsum; 6RRY; -.
DR PDBsum; 6RS0; -.
DR AlphaFoldDB; Q24451; -.
DR SMR; Q24451; -.
DR BioGRID; 66291; 3.
DR DIP; DIP-22953N; -.
DR IntAct; Q24451; 5.
DR STRING; 7227.FBpp0081509; -.
DR BindingDB; Q24451; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PaxDb; Q24451; -.
DR PRIDE; Q24451; -.
DR DNASU; 41126; -.
DR EnsemblMetazoa; FBtr0082031; FBpp0081509; FBgn0011740.
DR GeneID; 41126; -.
DR KEGG; dme:Dmel_CG18802; -.
DR CTD; 41126; -.
DR FlyBase; FBgn0011740; alpha-Man-IIa.
DR VEuPathDB; VectorBase:FBgn0011740; -.
DR eggNOG; KOG1958; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; Q24451; -.
DR OMA; GEMEIMQ; -.
DR PhylomeDB; Q24451; -.
DR BRENDA; 3.2.1.114; 1994.
DR SABIO-RK; Q24451; -.
DR SignaLink; Q24451; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 41126; 0 hits in 3 CRISPR screens.
DR ChiTaRS; alpha-Man-IIa; fly.
DR EvolutionaryTrace; Q24451; -.
DR GenomeRNAi; 41126; -.
DR PRO; PR:Q24451; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011740; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q24451; baseline and differential.
DR Genevisible; Q24451; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; NAS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0015923; F:mannosidase activity; IDA:FlyBase.
DR GO; GO:0004572; F:mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IMP:FlyBase.
DR GO; GO:0006517; P:protein deglycosylation; IDA:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0016063; P:rhodopsin biosynthetic process; IMP:FlyBase.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR041566; AManII_C.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF18230; Glyc_hyd_38C_2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycosidase; Golgi apparatus; Hydrolase;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..1108
FT /note="Alpha-mannosidase 2"
FT /id="PRO_0000206906"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..1108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 71
FT /note="E -> K (in Ref. 1; CAA54732)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..306
FT /note="QL -> HV (in Ref. 2; CAA10755)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> V (in Ref. 2; CAA10755)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="E -> K (in Ref. 1; CAA54732)"
FT /evidence="ECO:0000305"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6RRY"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 238..256
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6RRN"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 374..389
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 392..404
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 410..429
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 486..507
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 517..531
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 534..538
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 543..571
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 613..622
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 628..637
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 653..664
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 665..668
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 669..687
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 691..699
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:6RRH"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 711..715
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 757..761
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 763..766
FT /evidence="ECO:0007829|PDB:1QWN"
FT STRAND 769..778
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 794..797
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 817..823
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 826..836
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 838..843
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 851..859
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:3BVX"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 875..880
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 887..890
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 892..901
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 903..913
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 915..918
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 924..933
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 951..961
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 979..989
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 993..997
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1007..1009
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1020..1027
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1034..1044
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 1062..1064
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1065..1075
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1081..1085
FT /evidence="ECO:0007829|PDB:3BVX"
FT HELIX 1087..1089
FT /evidence="ECO:0007829|PDB:3BVX"
FT STRAND 1099..1107
FT /evidence="ECO:0007829|PDB:3BVX"
SQ SEQUENCE 1108 AA; 126721 MW; 55E370EC8CAC6D4A CRC64;
MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE LENGLQEHGE
EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD VPNVDVQMLE LYDRMSFKDI
DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP HSHNDPGWIQ TFEEYYQHDT KHILSNALRH
LHDNPEMKFI WAEISYFARF YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN
VLLQLTEGQT WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL
AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF KRMGSFGLSC
PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP LGDDFRFKQN TEWDVQRVNY
ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH QAERAGQAEF PTLSGDFFTY ADRSDNYWSG
YYTSRPYHKR MDRVLMHYVR AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT
AKTHVVVDYE QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE
DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP VEAQVSPVWS
WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS DSKPEHTSYA SNLLLRKNPT
SLPLGQYPED VKFGDPREIS LRVGNGPTLA FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV
RSHGDRSGAY LFLPNGPASP VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR
NLVDIGSLDN TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI
EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP VLHIYRLVLE
KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN EWIGAQGQFG GDHPSAREDL
DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC GTPEEHTQKL DVCHLLPNVA RCERTTLTFL
QNLEHLDGMV APEVCPMETA AYVSSHSS
